We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

2uy8

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2uy8.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2uy8.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2uy8| PDB=2uy8 | SCENE= }}
{{STRUCTURE_2uy8| PDB=2uy8 | SCENE= }}
-
'''R92A MUTANT OF BACILLUS SUBTILIS OXALATE DECARBOXYLASE OXDC'''
+
===R92A MUTANT OF BACILLUS SUBTILIS OXALATE DECARBOXYLASE OXDC===
-
==Overview==
+
<!--
-
Oxalate decarboxylase (EC 4.1.1.2) catalyses the conversion of oxalate into carbon dioxide and formate. It requires manganese and, uniquely, dioxygen for catalysis. It forms a homohexamer and each subunit contains two similar, but distinct, manganese sites termed sites 1 and 2. There is kinetic evidence that only site 1 is catalytically active and that site 2 is purely structural. However, the kinetics of enzymes with mutations in site 2 are often ambiguous and all mutant kinetics have been interpreted without structural information. Nine new site-directed mutants have been generated and four mutant crystal structures have now been solved. Most mutants targeted (i) the flexibility (T165P), (ii) favoured conformation (S161A, S164A, D297A or H299A) or (iii) presence (Delta162-163 or Delta162-164) of a lid associated with site 1. The kinetics of these mutants were consistent with only site 1 being catalytically active. This was particularly striking with D297A and H299A because they disrupted hydrogen bonds between the lid and a neighbouring subunit only when in the open conformation and were distant from site 2. These observations also provided the first evidence that the flexibility and stability of lid conformations are important in catalysis. The deletion of the lid to mimic the plant oxalate oxidase led to a loss of decarboxylase activity, but only a slight elevation in the oxalate oxidase side reaction, implying other changes are required to afford a reaction specificity switch. The four mutant crystal structures (R92A, E162A, Delta162-163 and S161A) strongly support the hypothesis that site 2 is purely structural.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17680775}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17680775 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17680775}}
==About this Structure==
==About this Structure==
Line 39: Line 43:
[[Category: Oxalate]]
[[Category: Oxalate]]
[[Category: R92a mutant]]
[[Category: R92a mutant]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 17:48:00 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 02:20:11 2008''

Revision as of 23:20, 27 July 2008

Image:2uy8.png

Template:STRUCTURE 2uy8

R92A MUTANT OF BACILLUS SUBTILIS OXALATE DECARBOXYLASE OXDC

Template:ABSTRACT PUBMED 17680775

About this Structure

2UY8 is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.

Reference

The identity of the active site of oxalate decarboxylase and the importance of the stability of active-site lid conformations., Just VJ, Burrell MR, Bowater L, McRobbie I, Stevenson CE, Lawson DM, Bornemann S, Biochem J. 2007 Nov 1;407(3):397-406. PMID:17680775

Page seeded by OCA on Mon Jul 28 02:20:11 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2uy8"
Personal tools